Reversible Redox Reconfiguration of Secondary Structures in a Designed Peptide

被引：25
作者：
Wang, Xiaojian [1 ]
Bergenfeld, Irina [1 ]
Arora, Paramjit S. [1 ]
Canary, James W. [1 ]
机构：
[1] NYU, Dept Chem, New York, NY 10003 USA
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2012年 / 51卷 / 48期
基金：
美国国家科学基金会;
关键词：
peptide switches; peptides; protein structures; redox chemistry; DE-NOVO DESIGN; AMYLOID FORMATION; SYNTHETIC BIOLOGY; COILED COILS; SOFT ACIDS; SWITCH; OLIGOPEPTIDE; BIOMATERIALS; CONVERSION; COMPLEXES;
D O I：
10.1002/anie.201206009
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Secondary structures are critical regulators of protein structure and function. Switchable peptides that can adopt multiple defined conformations in response to stimuli are attractive model systems for the study of protein folding and misfolding. A peptide is presented that can be reversibly reconfigured between an α-helical monomer and a β-sheet aggregate upon one-electron oxidation and reduction in the presence of Cu I/CuII. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码：12099 / 12101
页数：3
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